3wmd is a 2 chain structure with sequence from As 4.1619. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Multistep catalysis of epoxide hydrolase/cyclase in the epoxide opening cascade is an intriguing issue in polyether biosynthesis. A pair of structurally homologous epoxide hydrolases was found in gene clusters of ionophore polyethers. In the epoxide opening reactions with MonBI and MonBII involved in monensin biosynthesis, we found that MonBII and catalytically inactive MonBI mutant catalyzed two-step reactions of bisepoxide substrate analog to afford bicyclic product although MonBII alone catalyzed only the first cyclization. The X-ray crystal structure of MonBI dimers suggested the importance of the KSD motif in MonBI/MonBI interaction, which was further supported by gel filtration chromatography of wild-type MonBI and mutant MonBI. The involvement of the KSD motif in heterodimer formation was confirmed by in vitro assay. Direct evidence of MonBI/MonBII interaction was obtained by native mass spectrometry. Its dissociation constant was determined as 2.21x10-5 M by surface plasmon resonance. Our results suggested the involvement of an allosteric regulation mechanism by MonBI/MonBII interaction in monensin skeletal construction.
Allosteric regulation of epoxide opening cascades by a pair of epoxide hydrolases in monensin biosynthesis.,Minami A, Ose T, Sato K, Oikawa A, Kuroki K, Maenaka K, Oguri H, Oikawa H ACS Chem Biol. 2013 Dec 9. PMID:24320215[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Minami A, Ose T, Sato K, Oikawa A, Kuroki K, Maenaka K, Oguri H, Oikawa H. Allosteric regulation of epoxide opening cascades by a pair of epoxide hydrolases in monensin biosynthesis. ACS Chem Biol. 2013 Dec 9. PMID:24320215 doi:http://dx.doi.org/10.1021/cb4006485
